Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica
As insoluble substrates such as tapioca can be used to make chemical compounds, saccharification of tapioca by glucoamylase immobilised on mesostructured cellular foam (MCF) silica using Box-Behnken Design of experiment was conducted to optimize this process so that the experimental results can be u...
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al-Farabi Kazakh National University
2018-12-01
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Series: | Eurasian Chemico-Technological Journal |
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doaj-fa26bb41fa8d456e83d704e9adb839cb2020-11-24T23:32:57Zengal-Farabi Kazakh National UniversityEurasian Chemico-Technological Journal 1562-39202522-48672018-12-0120431131810.18321/ectj764764Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam SilicaJ. Agustian0L. Hermide1Department of Chemical Engineering, Universitas LampungDepartment of Chemical Engineering, Universitas LampungAs insoluble substrates such as tapioca can be used to make chemical compounds, saccharification of tapioca by glucoamylase immobilised on mesostructured cellular foam (MCF) silica using Box-Behnken Design of experiment was conducted to optimize this process so that the experimental results can be used to develop large-scale operations. The experiments gave dextrose equivalent (DE) values of 6.15–69.50% (w/w). Factors of pH and temperature affected the process highly. The suggested quadratic polynomial model is significant and considered acceptable (R2 = 99.78%). Justification of the model confirms its validity and adequacy where the predicted DE shows a good agreement with the experimental results. The kinetic constants (Vmax, KM) produced by the immobilised enzyme differed highly from the values yielded by free glucoamylase indicating reduction of substrate access to enzyme active sites had occurred.http://ect-journal.kz/index.php/ectj/article/view/764 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
J. Agustian L. Hermide |
spellingShingle |
J. Agustian L. Hermide Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica Eurasian Chemico-Technological Journal |
author_facet |
J. Agustian L. Hermide |
author_sort |
J. Agustian |
title |
Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica |
title_short |
Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica |
title_full |
Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica |
title_fullStr |
Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica |
title_full_unstemmed |
Saccharification Kinetics at Optimised Conditions of Tapioca by Glucoamylase Immobilised on Mesostructured Cellular Foam Silica |
title_sort |
saccharification kinetics at optimised conditions of tapioca by glucoamylase immobilised on mesostructured cellular foam silica |
publisher |
al-Farabi Kazakh National University |
series |
Eurasian Chemico-Technological Journal |
issn |
1562-3920 2522-4867 |
publishDate |
2018-12-01 |
description |
As insoluble substrates such as tapioca can be used to make chemical compounds, saccharification of tapioca by glucoamylase immobilised on mesostructured cellular foam (MCF) silica using Box-Behnken Design of experiment was conducted to optimize this process so that the experimental results can be used to develop large-scale operations. The experiments gave dextrose equivalent (DE) values of 6.15–69.50% (w/w). Factors of pH and temperature affected the process highly. The suggested quadratic polynomial model is significant and considered acceptable (R2 = 99.78%). Justification of the model confirms its validity and adequacy where the predicted DE shows a good agreement with the experimental results. The kinetic constants (Vmax, KM) produced by the immobilised enzyme differed highly from the values yielded by free glucoamylase indicating reduction of substrate access to enzyme active sites had occurred. |
url |
http://ect-journal.kz/index.php/ectj/article/view/764 |
work_keys_str_mv |
AT jagustian saccharificationkineticsatoptimisedconditionsoftapiocabyglucoamylaseimmobilisedonmesostructuredcellularfoamsilica AT lhermide saccharificationkineticsatoptimisedconditionsoftapiocabyglucoamylaseimmobilisedonmesostructuredcellularfoamsilica |
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